Sequence of MEMA_METCA

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
methane monooxygenase (soluble)
P22869
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
527
60646
Reaction
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
Sequences with same EC No.
Sequence
show sequence in fasta format
  0 MALSTATKAA TDALAANRAP TSVNAQEVHR WLQSFNWDFK NNRTKYATKY KMANETKEQF
 60 KLIAKEYARM EAVKDERQFG SLQDALTRLN AGVRVHPKWN ETMKVVSNFL EVGEYNAIAA
120 TGMLWDSAQA AEQKNGYLAQ VLDEIRHTHQ CAYVNYYFAK NGQDPAGHND ARRTRTIGPL
180 WKGMKRVFSD GFISGDAVEC SLNLQLVGEA CFTNPLIVAV TEWAAANGDE ITPTVFLSIE
240 TDELRHMANG YQTVVSIAND PASAKYLNTD LNNAFWTQQK YFTPVLGMLF EYGSKFKVEP
300 WVKTWNRWVY EDWGGIWIGR LGKYGVESPR SLKDAKQDAY WAHHDLYLLA YALWPTGFFR
360 LALPDQEEME WFEANYPGWY DHYGKIYEEW RARGCEDPSS GFIPLMWFIE NNHPIYIDRV
420 SQVPFCPSLA KGASTLRVHE YNGQMHTFSD QWGERMWLAE PERYECQNIF EQYEGRELSE
480 VIAELHGLRS DGKTLIAQPH VRGDKLWTLD DIKRLNCVFK NPVKAFN
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
675118
Stainthorpe A.C.,Lees V.,Salmond G.P.C.,Dalton H.,Murrell J.C.
The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath).
Gene
91
27-34
1990
675120
Ward N.L.,Larsen O.,Sakwa J.,Bruseth L.,Khouri H.M.,Durkin A.S.,Dimitrov G.,Jiang L.,Scanlan D.,Kang K.H.,Lewis M.R.,Nelson K.E.,Methe B.A.,Wu M.,Heidelberg J.F.,Paulsen I.T.,Fouts D.E.,Ravel J.,Tettelin H.,Ren Q.,Read T.D.,DeBoy R.T.,Seshadri R.,Salzberg S.L.,Jensen H.B.,Birkeland N.K.,Nelson W.C.,Dodson R.J.,Grindhaug S.H.,Holt I.E.,Eidhammer I.,Jonasen I.,Vanaken S.,Utterback T.R.,Feldblyum T.V.,Fraser C.M.,Lillehaug J.R.,Eisen J.A.
Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath).
PLoS Biol.
2
1616-1628
2004
675121
Rosenzweig A.C.,Frederick C.A.,Lippard S.J.,Nordlund P.
Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane.
Nature
366
537-543
1993
675122
Rosenzweig A.C.,Nordlund P.,Takahara P.M.,Frederick C.A.,Lippard S.J.
Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states.
Chem. Biol.
2
409-418
1995
675123
Rosenzweig A.C.,Brandstetter H.,Whittington D.A.,Nordlund P.,Lippard S.J.,Frederick C.A.
Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions.
Proteins
29
141-152
1997
675124
Whittington D.A.,Lippard S.J.
Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site.
J. Am. Chem. Soc.
123
827-838
2001